SCAM1_HUMAN
ID SCAM1_HUMAN Reviewed; 338 AA.
AC O15126; O43587; Q6FG23; Q96BX1; Q96QK5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Secretory carrier-associated membrane protein 1;
DE Short=Secretory carrier membrane protein 1;
GN Name=SCAMP1; Synonyms=SCAMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9378760; DOI=10.1242/jcs.110.17.2099;
RA Singleton D.R., Wu T.T., Castle J.D.;
RT "Three mammalian SCAMPs (secretory carrier membrane proteins) are highly
RT related products of distinct genes having similar subcellular
RT distributions.";
RL J. Cell Sci. 110:2099-2107(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A7.
RX PubMed=15840657; DOI=10.1242/jcs.02315;
RA Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.;
RT "Secretory carrier membrane proteins interact and regulate trafficking of
RT the organellar (Na+,K+)/H+ exchanger NHE7.";
RL J. Cell Sci. 118:1885-1897(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with SYNRG and ITSN1 (By similarity). Interacts with
CC SLC9A7. {ECO:0000250, ECO:0000269|PubMed:15840657}.
CC -!- INTERACTION:
CC O15126; P53367: ARFIP1; NbExp=3; IntAct=EBI-954338, EBI-2808808;
CC O15126; P53365: ARFIP2; NbExp=3; IntAct=EBI-954338, EBI-638194;
CC O15126; P55212: CASP6; NbExp=3; IntAct=EBI-954338, EBI-718729;
CC O15126; Q05329: GAD2; NbExp=3; IntAct=EBI-954338, EBI-9304251;
CC O15126; P13473-2: LAMP2; NbExp=3; IntAct=EBI-954338, EBI-21591415;
CC O15126; Q96E29: MTERF3; NbExp=3; IntAct=EBI-954338, EBI-7825321;
CC O15126; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-954338, EBI-11978907;
CC O15126; Q96AL5: PBX3; NbExp=3; IntAct=EBI-954338, EBI-741171;
CC O15126; P49585: PCYT1A; NbExp=3; IntAct=EBI-954338, EBI-2563309;
CC O15126; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-954338, EBI-5280197;
CC O15126; P43378: PTPN9; NbExp=3; IntAct=EBI-954338, EBI-742898;
CC O15126; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-954338, EBI-2623095;
CC O15126; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-954338, EBI-742688;
CC O15126; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-954338, EBI-10172380;
CC O15126; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-954338, EBI-702328;
CC O15126; Q8WY91: THAP4; NbExp=3; IntAct=EBI-954338, EBI-726691;
CC O15126; P49638: TTPA; NbExp=3; IntAct=EBI-954338, EBI-10210710;
CC O15126; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-954338, EBI-10182121;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15840657}. Recycling endosome membrane
CC {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15840657}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15126-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15126-2; Sequence=VSP_004380;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; AF005037; AAB62722.1; -; mRNA.
DR EMBL; AF038966; AAC39864.1; -; mRNA.
DR EMBL; CR542286; CAG47081.1; -; mRNA.
DR EMBL; BC009787; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471084; EAW95814.1; -; Genomic_DNA.
DR EMBL; BC015065; AAH15065.1; -; mRNA.
DR EMBL; BC034048; AAH34048.1; -; mRNA.
DR CCDS; CCDS75264.1; -. [O15126-1]
DR RefSeq; NP_001277158.1; NM_001290229.1.
DR RefSeq; NP_004857.4; NM_004866.5. [O15126-1]
DR AlphaFoldDB; O15126; -.
DR SMR; O15126; -.
DR BioGRID; 114899; 135.
DR CORUM; O15126; -.
DR IntAct; O15126; 54.
DR MINT; O15126; -.
DR STRING; 9606.ENSP00000481022; -.
DR TCDB; 8.A.103.1.1; the secretory carrier-associated membrane protein (scamp) family.
DR iPTMnet; O15126; -.
DR MetOSite; O15126; -.
DR PhosphoSitePlus; O15126; -.
DR SwissPalm; O15126; -.
DR BioMuta; SCAMP1; -.
DR EPD; O15126; -.
DR jPOST; O15126; -.
DR MassIVE; O15126; -.
DR MaxQB; O15126; -.
DR PeptideAtlas; O15126; -.
DR PRIDE; O15126; -.
DR ProteomicsDB; 48463; -. [O15126-1]
DR ProteomicsDB; 48464; -. [O15126-2]
DR Antibodypedia; 24511; 161 antibodies from 25 providers.
DR DNASU; 9522; -.
DR Ensembl; ENST00000614488.4; ENSP00000478071.1; ENSG00000085365.18. [O15126-2]
DR Ensembl; ENST00000621999.5; ENSP00000481022.1; ENSG00000085365.18. [O15126-1]
DR GeneID; 9522; -.
DR KEGG; hsa:9522; -.
DR MANE-Select; ENST00000621999.5; ENSP00000481022.1; NM_004866.6; NP_004857.4.
DR UCSC; uc032uzx.2; human. [O15126-1]
DR CTD; 9522; -.
DR DisGeNET; 9522; -.
DR GeneCards; SCAMP1; -.
DR HGNC; HGNC:10563; SCAMP1.
DR HPA; ENSG00000085365; Low tissue specificity.
DR MIM; 606911; gene.
DR neXtProt; NX_O15126; -.
DR OpenTargets; ENSG00000085365; -.
DR PharmGKB; PA34976; -.
DR VEuPathDB; HostDB:ENSG00000085365; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000157310; -.
DR HOGENOM; CLU_066546_0_1_1; -.
DR InParanoid; O15126; -.
DR OMA; NMVACIF; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; O15126; -.
DR PathwayCommons; O15126; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O15126; -.
DR SIGNOR; O15126; -.
DR BioGRID-ORCS; 9522; 6 hits in 245 CRISPR screens.
DR ChiTaRS; SCAMP1; human.
DR GeneWiki; SCAMP1; -.
DR GenomeRNAi; 9522; -.
DR Pharos; O15126; Tbio.
DR PRO; PR:O15126; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15126; protein.
DR Bgee; ENSG00000085365; Expressed in pigmented layer of retina and 217 other tissues.
DR ExpressionAtlas; O15126; baseline and differential.
DR Genevisible; O15126; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0042589; C:zymogen granule membrane; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..338
FT /note="Secretory carrier-associated membrane protein 1"
FT /id="PRO_0000191250"
FT TOPO_DOM 2..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..261
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56603"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 158..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004380"
FT CONFLICT 119
FT /note="N -> I (in Ref. 2; AAC39864)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="D -> E (in Ref. 2; AAC39864)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="W -> L (in Ref. 1; AAB62722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37920 MW; C5745732744BE3C7 CRC64;
MSDFDSNPFA DPDLNNPFKD PSVTQVTRNV PPGLDEYNPF SDSRTPPPGG VKMPNVPNTQ
PAIMKPTEEH PAYTQIAKEH ALAQAELLKR QEELERKAAE LDRREREMQN LSQHGRKNNW
PPLPSNFPVG PCFYQDFSVD IPVEFQKTVK LMYYLWMFHA VTLFLNIFGC LAWFCVDSAR
AVDFGLSILW FLLFTPCSFV CWYRPLYGAF RSDSSFRFFV FFFVYICQFA VHVLQAAGFH
NWGNCGWISS LTGLNQNIPV GIMMIIIAAL FTASAVISLV MFKKVHGLYR TTGASFEKAQ
QEFATGVMSN KTVQTAAANA ASTAASSAAQ NAFKGNQI
